ArticleBMC biochemistry2018
Feruloyl esterase immobilization in mesoporous silica particles and characterization in hydrolysis and transesterification.
Article in BMC biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 40 citations in OpenAlex.
- Trends in the Use of Lipases: A Systematic Review and Bibliometric Analysis.Foods (Basel, Switzerland) · 2023Review
- Feruloyl Esterase (International journal of molecular sciences · 2023Article
- Article
- Review
- Approaches for the enzymatic synthesis of alkyl hydroxycinnamates and applications thereof.Applied microbiology and biotechnology · 2021Review
- Effects of Pore Size and Crosslinking Methods on the Immobilization of Myoglobin in SBA-15.Frontiers in bioengineering and biotechnology · 2021Article
- Optimization of fermentation conditions for the production of recombinant feruloyl esterase from3 Biotech · 2020Article
- Multimodular fused acetyl-feruloyl esterases from soil and gut Bacteroidetes improve xylanase depolymerization of recalcitrant biomass.Biotechnology for biofuels · 2020Article
- Glycosylation influences activity, stability and immobilization of the feruloyl esterase 1a from Myceliophthora thermophila.AMB Express · 2019Article
- Optimized Enzymatic Synthesis of Feruloyl Derivatives Catalyzed by Three Novel Feruloyl Esterases fromComputational and structural biotechnology journal · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
backgroundEnzymes display high reactivity and selectivity under natural conditions, but may suffer from decreased efficiency in industrial applications. A strategy to address this limitation is to immobilize the enzyme. Mesoporous silica materials offer unique properties as an immobilization support, such as high surface area and tunable pore size.
resultsThe performance of a commercially available feruloyl esterase, E-FAERU, immobilized on mesoporous silica by physical adsorption was evaluated for its transesterification ability. We optimized the immobilization conditions by varying the support pore size, the immobilization buffer and its pH. Maximum loading and maximum activity were achieved at different pHs (4.0 and 6.0 respectively). Selectivity, shown by the transesterification/hydrolysis products molar ratio, varied more than 3-fold depending on the reaction buffer used and its pH. Under all conditions studied, hydrolysis was the dominant activity of the enzyme. pH and water content had the greatest influence on the enzyme selectivity and activity. Determined kinetic parameters of the enzyme were obtained and showed that K
conclusionsThese results indicate that this enzyme is more suited for hydrolysis reactions than transesterification despite good reusability. Furthermore, it was found that the immobilization conditions are crucial for optimal enzyme activity as they can alter the enzyme performance.
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